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| - | Crystal structure of a large fragment of human type II topoisomerases (TOP2) complexed to DNA and to the anticancer drug etoposide to reveal structural details of drug-induced stabilization of a cleavage complex. The interplay between the protein, the DNA, and the drug explains the structure-activity relations of etoposide derivatives and the molecular basis of drug-resistant mutations. | + | Crystal structure of a large fragment of human type II topoisomerases (TOP2) complexed to DNA and to the anticancer drug etoposide to reveal structural details of drug-induced stabilization of a cleavage complex<ref>PMID: 21778401</ref>. The interplay between the protein, the DNA, and the drug explains the structure-activity relations of etoposide derivatives and the molecular basis of drug-resistant mutations. |
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==References== | ==References== | ||
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Revision as of 02:40, 19 September 2012
Human topoisomerase IIbeta in complex with DNA and etoposide
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Crystal structure of a large fragment of human type II topoisomerases (TOP2) complexed to DNA and to the anticancer drug etoposide to reveal structural details of drug-induced stabilization of a cleavage complex[1]. The interplay between the protein, the DNA, and the drug explains the structure-activity relations of etoposide derivatives and the molecular basis of drug-resistant mutations.
References
- ↑ Wu CC, Li TK, Farh L, Lin LY, Lin TS, Yu YJ, Yen TJ, Chiang CW, Chan NL. Structural basis of type II topoisomerase inhibition by the anticancer drug etoposide. Science. 2011 Jul 22;333(6041):459-62. PMID:21778401 doi:10.1126/science.1204117
